α-/γ-Taxilin are required for centriolar subdistal appendage assembly and microtubule organization

Elife. 2022 Feb 4:11:e73252. doi: 10.7554/eLife.73252.

Abstract

The centrosome composed of a pair of centrioles (mother and daughter) and pericentriolar material, and is mainly responsible for microtubule nucleation and anchorage in animal cells. The subdistal appendage (SDA) is a centriolar structure located at the mother centriole's subdistal region, and it functions in microtubule anchorage. However, the molecular composition and detailed structure of the SDA remain largely unknown. Here, we identified α-taxilin and γ-taxilin as new SDA components that form a complex via their coiled-coil domains and that serve as a new subgroup during SDA hierarchical assembly. The taxilins' SDA localization is dependent on ODF2, and α-taxilin recruits CEP170 to the SDA. Functional analyses suggest that α- and γ-taxilin are responsible for SDA structural integrity and centrosomal microtubule anchorage during interphase and for proper spindle orientation during metaphase. Our results shed light on the molecular components and functional understanding of the SDA hierarchical assembly and microtubule organization.

Keywords: cell biology; centrosome; human; microtubule; super-high resolution.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Biological Phenomena
  • Cell Line
  • Cell Line, Tumor
  • Centrioles / metabolism*
  • Heat-Shock Proteins / metabolism*
  • Humans
  • Microtubule-Associated Proteins / metabolism*
  • Microtubules / metabolism
  • Protein Domains
  • Vesicular Transport Proteins / metabolism*

Substances

  • Cep170 protein, human
  • Heat-Shock Proteins
  • Microtubule-Associated Proteins
  • ODF2 protein, human
  • TXLNA protein, human
  • TXLNG protein, human
  • Vesicular Transport Proteins

Grants and funding

The funders had no role in study design, data collection and interpretation, or the decision to submit the work for publication.